Final published version
Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
}
TY - JOUR
T1 - BSD2 is a Rubisco-specific assembly chaperone, forms intermediary hetero-oligomeric complexes, and is nonlimiting to growth in tobacco
AU - Conlan, B.
AU - Birch, R.
AU - Kelso, C.
AU - Holland, S.
AU - De Souza, A.P.
AU - Long, S.P.
AU - Beck, J.L.
AU - Whitney, S.M.
PY - 2019/4/1
Y1 - 2019/4/1
N2 - The folding and assembly of Rubisco large and small subunits into L 8 S 8 holoenzyme in chloroplasts involves many auxiliary factors, including the chaperone BSD2. Here we identify apparent intermediary Rubisco-BSD2 assembly complexes in the model C 3 plant tobacco. We show BSD2 and Rubisco content decrease in tandem with leaf age with approximately half of the BSD2 in young leaves (~70 nmol BSD2 protomer.m 2 ) stably integrated in putative intermediary Rubisco complexes that account for <0.2% of the L 8 S 8 pool. RNAi-silencing BSD2 production in transplastomic tobacco producing bacterial L 2 Rubisco had no effect on leaf photosynthesis, cell ultrastructure, or plant growth. Genetic crossing the same RNAi-bsd2 alleles into wild-type tobacco however impaired L 8 S 8 Rubisco production and plant growth, indicating the only critical function of BSD2 is in Rubisco biogenesis. Agrobacterium mediated transient expression of tobacco, Arabidopsis, or maize BSD2 reinstated Rubisco biogenesis in BSD2-silenced tobacco. Overexpressing BSD2 in tobacco chloroplasts however did not alter Rubisco content, activation status, leaf photosynthesis rate, or plant growth in the field or in the glasshouse at 20°C or 35°C. Our findings indicate BSD2 functions exclusively in Rubisco biogenesis, can efficiently facilitate heterologous plant Rubisco assembly, and is produced in amounts nonlimiting to tobacco growth.
AB - The folding and assembly of Rubisco large and small subunits into L 8 S 8 holoenzyme in chloroplasts involves many auxiliary factors, including the chaperone BSD2. Here we identify apparent intermediary Rubisco-BSD2 assembly complexes in the model C 3 plant tobacco. We show BSD2 and Rubisco content decrease in tandem with leaf age with approximately half of the BSD2 in young leaves (~70 nmol BSD2 protomer.m 2 ) stably integrated in putative intermediary Rubisco complexes that account for <0.2% of the L 8 S 8 pool. RNAi-silencing BSD2 production in transplastomic tobacco producing bacterial L 2 Rubisco had no effect on leaf photosynthesis, cell ultrastructure, or plant growth. Genetic crossing the same RNAi-bsd2 alleles into wild-type tobacco however impaired L 8 S 8 Rubisco production and plant growth, indicating the only critical function of BSD2 is in Rubisco biogenesis. Agrobacterium mediated transient expression of tobacco, Arabidopsis, or maize BSD2 reinstated Rubisco biogenesis in BSD2-silenced tobacco. Overexpressing BSD2 in tobacco chloroplasts however did not alter Rubisco content, activation status, leaf photosynthesis rate, or plant growth in the field or in the glasshouse at 20°C or 35°C. Our findings indicate BSD2 functions exclusively in Rubisco biogenesis, can efficiently facilitate heterologous plant Rubisco assembly, and is produced in amounts nonlimiting to tobacco growth.
KW - chaperone
KW - photosynthesis
KW - protein folding
KW - RuBP carboxylation
KW - bacterium
KW - biochemical composition
KW - chloroplast
KW - enzyme
KW - enzyme activity
KW - gene expression
KW - genetic engineering
KW - growth
KW - limiting factor
KW - polymer
KW - protein
KW - tobacco
KW - ultrastructure
KW - Agrobacterium
KW - Arabidopsis
KW - Bacteria (microorganisms)
KW - Nicotiana tabacum
KW - Zea mays
U2 - 10.1111/pce.13473
DO - 10.1111/pce.13473
M3 - Journal article
VL - 42
SP - 1287
EP - 1301
JO - Plant, Cell and Environment
JF - Plant, Cell and Environment
SN - 0140-7791
IS - 4
ER -